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| {{STRUCTURE_2p99| PDB=2p99 | SCENE= }} | | {{STRUCTURE_2p99| PDB=2p99 | SCENE= }} |
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| '''E. coli methionine aminopeptidase monometalated with inhibitor YE6'''
| | ===E. coli methionine aminopeptidase monometalated with inhibitor YE6=== |
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| ==Overview==
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| Two divalent metal ions are commonly seen in the active-site cavity of methionine aminopeptidase, and at least one of the metal ions is directly involved in catalysis. Although ample structural and functional information is available for dimetalated enzyme, methionine aminopeptidase likely functions as a monometalated enzyme under physiological conditions. Information on structure, as well as catalysis and inhibition, of the monometalated enzyme is lacking. By improving conditions of high-throughput screening, we identified a unique inhibitor with specificity toward the monometalated enzyme. Kinetic characterization indicates a mutual exclusivity in binding between the inhibitor and the second metal ion at the active site. This is confirmed by X-ray structure, and this inhibitor coordinates with the first metal ion and occupies the space normally occupied by the second metal ion. Kinetic and structural analyses of the inhibition by this and other inhibitors provide insight in designing effective inhibitors of methionine aminopeptidase.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17948983}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17948983 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17948983}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Monometalated]] | | [[Category: Monometalated]] |
| [[Category: Mononuclear]] | | [[Category: Mononuclear]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:39:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:22:35 2008'' |